Nuclear‐Magnetic‐Resonance Studies of Ferrocytochrome c

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Abstract
The pH dependence and the temperature dependence of the nuclear magnetic resonance spectrum of horse ferrocytochrome c are described. This protein is very stable; it maintains an ordered structure over the pH range 4 to 12 at 25 °C and over the temperature range 4°C to 97 °C at pH 7.0. The dynamic characteristics of the conformation of ferrocytochrome c were investigated. Particular emphasis was laid on the aromatic resonances and resonances of methyl groups shifted far upheld. Tyr‐48 and Phe‐46 were found to be relatively immobile whilst a region of the protein close to Ile‐57 was found to be relatively flexible.